1.11.1.19: dye decolorizing peroxidase

This is an abbreviated version, for detailed information about dye decolorizing peroxidase, go to the full flat file.

Reaction

Reactive Blue 5
+ 2 H2O2 =
Phthalate
+
2,2'-disulfonyl azobenzene
+
3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate
+ 2 H2O

Synonyms

AnaPX, dye-decolorizing peroxidase, DyP, DyP I, DyP II, DyP-I, DyP-type peroxidase, DyP1, DyP2, DyP3, EfeB, LiP BA45, LiP-SN, manganese-independent peroxidase I, manganese-independent peroxidase II, TT1485, tyrA, YcdB, YfeX, YwbN

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.19 dye decolorizing peroxidase

Engineering

Engineering on EC 1.11.1.19 - dye decolorizing peroxidase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M401F
-
heme cavity mutant with significantly increased H2O2 stability of 8.2fold, the mutant retains 16% activity at 100 mM H2O2
M401I
-
heme cavity mutant with significantly increased H2O2 stability of 3.7fold
M401L
-
heme cavity mutant with significantly increased H2O2 stability of 2.4fold
M451I
-
heme cavity mutant with significantly increased H2O2 stability of 5.2fold, the mutant retains 5% activity at 100 mM H2O2
G169L
-
the mutant shows strongly increased activity compared to the wild type enzyme
Y147F/Y337F
-
the mutant shows reduced activity compared to the wild type enzyme
Y147S
-
the mutant shows reduced activity compared to the wild type enzyme
Y337S
-
the mutant shows about wild type activity
D143A
-
the mutant shows no activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and guaiacol, but about 20% of wild type activity with Reactive Blue 19 and 10% activity with catechol
D143N
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
H215A
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
L246W
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
R232E
-
the mutant shows no activity towards Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), but about 40% of wild type activity with guaiacol and 35% activity with catechol
R232L
-
the mutant shows no activity towards Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), but about 90% of wild type activity with guaiacol and 50% activity with catechol
S234Y
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
D143A
-
the mutant shows no activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and guaiacol, but about 20% of wild type activity with Reactive Blue 19 and 10% activity with catechol
-
D143N
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
H215A
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
R232E
-
the mutant shows no activity towards Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), but about 40% of wild type activity with guaiacol and 35% activity with catechol
-
R232L
-
the mutant shows no activity towards Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), but about 90% of wild type activity with guaiacol and 50% activity with catechol
-
H164A
-
DyP activity and heme binding are lost in the H164A mutant
E188K
-
the mutant shows 3-4fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
E188K/A142V
-
the mutant shows 2fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
E188K/A142V/H125Y
-
the mutant shows a 100fold enhanced catalytic efficiency (kcat/Km) for 2,6-dimethoxyphenol and 2fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
E188K/H125R
-
the mutant shows 6fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
H125R
-
the mutant shows 3-4fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
E188K
-
the mutant shows 3-4fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
-
E188K/A142V
-
the mutant shows 2fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
-
E188K/A142V/H125Y
-
the mutant shows a 100fold enhanced catalytic efficiency (kcat/Km) for 2,6-dimethoxyphenol and 2fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
-
E188K/H125R
-
the mutant shows 6fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
-
H125R
-
the mutant shows 3-4fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
-
D171N
-
the mutant displays 3000fold less enzymatic activity compared to the wild type DyP
H164A
-
the specific activity of the purified mutant is 99.8% lower than that of recombinant DyP expressed in Escherichia coli
H166A
-
the specific activity of the purified mutant is 95% lower than that of recombinant DyP expressed in Escherichia coli
D242A
the mutant shows 0.7% of the Reactive Blue 19-decolorizing activity of the wild type protein
H338A
the mutant lacks the heme cofactor and shows 3% of the Reactive Blue 19-decolorizing activity of the wild type protein
D220A
the catalytic efficiency of the mutant toward H2O2 drops by 22fold compared to the wild type enzyme
D220F
the mutant shows reduced activity compared to the wild type enzyme
D220G
the mutant shows reduced activity compared to the wild type enzyme
D220H
the mutant shows reduced activity compared to the wild type enzyme
D220K
the mutant shows reduced activity compared to the wild type enzyme
D220N
the mutant shows reduced activity compared to the wild type enzyme
H312C
the catalytic efficiency of the mutant toward H2O2 drops by 88fold compared to the wild type enzyme
D220A
-
the catalytic efficiency of the mutant toward H2O2 drops by 22fold compared to the wild type enzyme
-
D220N
-
the mutant shows reduced activity compared to the wild type enzyme
-
H312C
-
the catalytic efficiency of the mutant toward H2O2 drops by 88fold compared to the wild type enzyme
-